Inhibition of UBE2D3 expression attenuates radiosensitivity of MCF-7 human breast cancer cells by increasing hTERT expression and activity

PLoS One. 2013 May 31;8(5):e64660. doi: 10.1371/journal.pone.0064660. Print 2013.

Abstract

The known functions of telomerase in tumor cells include replenishing telomeric DNA and maintaining cell immortality. We have previously shown the existence of a negative correlation between human telomerase reverse transcriptase (hTERT) and radiosensitivity in tumor cells. Here we set out to elucidate the molecular mechanisms underlying regulation by telomerase of radiosensitivity in MCF-7 cells. Toward this aim, yeast two-hybrid (Y2H) screening of a human laryngeal squamous cell carcinoma radioresistant (Hep2R) cDNA library was first performed to search for potential hTERT interacting proteins. We identified ubiquitin-conjugating enzyme E2D3 (UBE2D3) as a principle hTERT-interacting protein and validated this association biochemically. ShRNA-mediated inhibition of UBE2D3 expression attenuated MCF-7 radiosensitivity, and induced the accumulation of hTERT and cyclin D1 in these cells. Moreover, down-regulation of UBE2D3 increased hTERT activity and cell proliferation, accelerating G1 to S phase transition in MCF-7 cells. Collectively these findings suggest that UBE2D3 participates in the process of hTERT-mediated radiosensitivity in human breast cancer MCF-7 cells by regulating hTERT and cyclin D1.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line, Tumor
  • Cell Proliferation
  • Cyclin D1 / genetics*
  • Cyclin D1 / metabolism
  • Female
  • Gamma Rays
  • Gene Expression Regulation, Neoplastic*
  • Gene Library
  • Humans
  • RNA, Small Interfering / genetics
  • RNA, Small Interfering / metabolism
  • Radiation Tolerance / genetics*
  • Signal Transduction
  • Telomerase / genetics*
  • Telomerase / metabolism
  • Two-Hybrid System Techniques
  • Ubiquitin-Conjugating Enzymes / antagonists & inhibitors
  • Ubiquitin-Conjugating Enzymes / genetics*
  • Ubiquitin-Conjugating Enzymes / metabolism

Substances

  • RNA, Small Interfering
  • Cyclin D1
  • UBE2D3 protein, human
  • Ubiquitin-Conjugating Enzymes
  • TERT protein, human
  • Telomerase

Grants and funding

This work was supported by the National Basic Research Program of China (No.2009CB526410) and National Natural Science Foundation of China (No.81071825). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.